Hydrogenase activity of mineral-associated and suspended populations of Desulfovibrio desulfuricans Essex 6

dc.contributor.authorReardon, Catherine L.
dc.contributor.authorMagnuson, Timothy S.
dc.contributor.authorBoyd, Eric S.
dc.contributor.authorLeavitt, W. D.
dc.contributor.authorReed, D. W.
dc.contributor.authorGeesey, Gill G.
dc.date.accessioned2016-12-05T23:13:47Z
dc.date.available2016-12-05T23:13:47Z
dc.date.issued2014-02
dc.description.abstractThe interactions between sulfate-reducing microorganisms and iron oxides influence a number of important redox-sensitive biogeochemical processes including the formation of iron sulfides. Enzymes, such as hydrogenase which catalyze the reversible oxidation of molecular hydrogen, are known to mediate electron transfer to metals and may contribute to the formation and speciation of ferrous sulfides formed at the cell–mineral interface. In the present study, we compared the whole cell hydrogenase activity of Desulfovibrio desulfuricans strain Essex 6 growing as biofilms on hematite (hematite-associated) or as suspended populations using different metabolic pathways. Hematite-associated cells exhibited significantly greater hydrogenase activity than suspended populations during sulfate respiration but not during pyruvate fermentation. The enhanced activity of the hematite-associated, sulfate-grown cells appears to be dependent on iron availability rather than a general response to surface attachment since the activity of glass-associated cells did not differ from that of suspended populations. Hydrogenase activity of pyruvate-fermenting cells was stimulated by addition of iron as soluble Fe(II)Cl2 and, in the absence of added iron, both sulfate-reducing and pyruvate-fermenting cells displayed similar rates of hydrogenase activity. These data suggest that iron exerts a stronger influence on whole cell hydrogenase activity than either metabolic pathway or mode of growth. The location of hydrogenase to the cell envelope and the enhanced activity at the hematite surface in sulfate-reducing cells may influence the redox conditions that control the species of iron sulfides on the mineral surface.en_US
dc.description.sponsorshipInland Northwest Research Alliance grant MSU003en_US
dc.identifier.citationReardon CL, Magnuson TS, Boyd ES, Leavitt WD, Reed DW, Geesey GG, "Hydrogenase activity of mineral-associated and suspended populations of Desulfovibrio desulfuricans Essex 6," Microbial Ecology, 67(2):318–326.en_US
dc.identifier.issn0095-3628
dc.identifier.urihttps://scholarworks.montana.edu/handle/1/12325
dc.titleHydrogenase activity of mineral-associated and suspended populations of Desulfovibrio desulfuricans Essex 6en_US
dc.typeArticleen_US
mus.citation.extentfirstpage318en_US
mus.citation.extentlastpage326en_US
mus.citation.issue2en_US
mus.citation.journaltitleMicrobial Ecologyen_US
mus.citation.volume67en_US
mus.data.thumbpage8en_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1007/s00248-013-0308-yen_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US

Files

Original bundle

Now showing 1 - 1 of 1
Thumbnail Image
Name:
14-008_Hydrogenase_activity_mineral-assoc__A1b.pdf
Size:
372.1 KB
Format:
Adobe Portable Document Format
Description:
Hydrogenase activity of mineral-associated and suspended populations of Desulfovibrio desulfuricans Essex 6 (PDF)

License bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
826 B
Format:
Item-specific license agreed upon to submission
Description:
Copyright (c) 2002-2022, LYRASIS. All rights reserved.